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• W2078586023 abstract "1-Methyl-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline (salsolinol), an endogenous neurotoxin present in the mammalian brain, is known to perform a role in the pathogenesis of Parkinson's disease. In this study, we evaluated oxidative modifications of ferritin occurring after incubation with salsolinol. When ferritin was incubated with salsolinol, protein aggregation increased in a time-dependent manner. Free radical scavengers inhibited this salsolinol-mediated ferritin modification. The exposure of ferritin to salsolinol also results in the generation of protein carbonyl compounds and the formation of dityrosine. The results of this study show that free radicals may perform a pivotal role in salsolinol-mediated ferritin modification. Histidine dipeptides, such as carnosine, have been proposed to function as antioxidant agents in vivo. In this study, we also attempted to determine whether the histidine dipeptides, carnosine and N-acetyl-carnosine, could prevent salsolinol-mediated oxidative modification of ferritin. Our results showed that both carnosine and N-acetyl-carnosine significantly reduced ferritin aggregation. Both compounds effectively inhibited the formation of both carbonyl compounds and dityrosine. These results suggest that carnosine derivatives can, indeed, protect against salsolinol-mediated ferritin modification, as the consequence of free radical-scavenging activity." @default.
• W2078586023 created "2016-06-24" @default.
• W2078586023 creator A5055316697 @default.
• W2078586023 date "2010-05-01" @default.
• W2078586023 modified "2023-09-27" @default.
• W2078586023 title "Salsolinol, a catechol neurotoxin, induces modification of ferritin: Protection by histidine dipeptide" @default.
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• W2078586023 doi "https://doi.org/10.1016/j.etap.2010.01.007" @default.
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